RAB3A Interacting Protein Like 1 (RAB3IL1), also known as Guanine Nucleotide Exchange Factor for Rab-3A (GRAB), is a protein encoded by the RAB3IL1 gene in humans. This protein is a member of the SEC2 family and plays a crucial role in the regulation of synaptic vesicle exocytosis by activating Rab3A, a GTPase .
RAB3IL1 functions as a guanine nucleotide exchange factor (GEF) for Rab3A. It promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form . This activation is essential for the regulation of vesicle-mediated transport and Rab regulation of trafficking . Additionally, RAB3IL1 may also activate other Rab proteins such as RAB8A and RAB8B .
RAB3IL1 is expressed in various tissues, including lymphoid tissue, bone marrow, testis, and skeletal muscle . It is involved in several biological processes such as protein ubiquitination, immune response, and spermatid development . The protein interacts with multiple other proteins, indicating its involvement in complex cellular pathways .
Mutations or dysregulation of the RAB3IL1 gene have been associated with certain diseases, including Spinal Muscular Atrophy with Lower Extremity Predominant 1 . Understanding the function and regulation of RAB3IL1 can provide insights into the molecular mechanisms underlying these conditions and potentially lead to the development of targeted therapies.
Human recombinant RAB3IL1 is used in various research applications to study its role in cellular processes and disease mechanisms. The recombinant protein is produced using advanced biotechnological methods to ensure high purity and activity . Researchers utilize this protein to investigate its interactions, regulatory mechanisms, and potential therapeutic applications.